EC Number | Cloned (Comment) | Organism |
---|---|---|
6.2.1.33 | DNA sequence determination, expression of the His-tagged enzyme in Escherichia coli strain JM109 | Alcaligenes sp. |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
6.2.1.33 | purified recombinant enzyme, X-ray diffraction structure determination and analysis, modelling | Alcaligenes sp. |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
6.2.1.33 | D385A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Alcaligenes sp. |
6.2.1.33 | E410A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Alcaligenes sp. |
6.2.1.33 | F473A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzymem but increased kcat | Alcaligenes sp. |
6.2.1.33 | G408A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Alcaligenes sp. |
6.2.1.33 | H207A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Alcaligenes sp. |
6.2.1.33 | H207F | site-directed mutagenesis,the mutant shows reduced activity compared to the wild-type enzyme | Alcaligenes sp. |
6.2.1.33 | H207Q | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Alcaligenes sp. |
6.2.1.33 | H254A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Alcaligenes sp. |
6.2.1.33 | K477A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Alcaligenes sp. |
6.2.1.33 | K492A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Alcaligenes sp. |
6.2.1.33 | K492L | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Alcaligenes sp. |
6.2.1.33 | K492R | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Alcaligenes sp. |
6.2.1.33 | M203A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Alcaligenes sp. |
6.2.1.33 | N302A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Alcaligenes sp. |
6.2.1.33 | R400A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Alcaligenes sp. |
6.2.1.33 | R439A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Alcaligenes sp. |
6.2.1.33 | R475A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Alcaligenes sp. |
6.2.1.33 | R87A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Alcaligenes sp. |
6.2.1.33 | S407A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Alcaligenes sp. |
6.2.1.33 | T161A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Alcaligenes sp. |
6.2.1.33 | T251A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Alcaligenes sp. |
6.2.1.33 | T306A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Alcaligenes sp. |
6.2.1.33 | T307A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Alcaligenes sp. |
6.2.1.33 | W440A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, but increased kcat | Alcaligenes sp. |
6.2.1.33 | Y304F | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Alcaligenes sp. |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
6.2.1.33 | 4-chlorophenacyl-CoA | a product analogue, noncompetitive versus 4-methylbenzoate and ATP, dead-end inhibitor | Alcaligenes sp. | |
6.2.1.33 | AMP | is a noncompetitive inhibitor versus ATP and an uncompetitive versus CoA | Alcaligenes sp. | |
6.2.1.33 | diphosphate | competitive versus ATP | Alcaligenes sp. |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
6.2.1.33 | additional information | - |
additional information | transient-state and steady-state kinetics of wild-type and mutant enzymes, overview | Alcaligenes sp. |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
6.2.1.33 | Mg2+ | - |
Alcaligenes sp. |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.2.1.33 | 4-Chlorobenzoate + CoA + ATP | Alcaligenes sp. | - |
4-Chlorobenzoyl-CoA + AMP + diphosphate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
6.2.1.33 | Alcaligenes sp. | Q8GN86 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
6.2.1.33 | recombinant His-tagged enzyme from Escherichia coli strain JM109 by nickel affinity chromatography | Alcaligenes sp. |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
6.2.1.33 | 4-Chlorobenzoate + CoA + ATP = 4-chlorobenzoyl-CoA + AMP + diphosphate | kinetic reaction mechanism, overview | Alcaligenes sp. |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.2.1.33 | 4-Chlorobenzoate + CoA + ATP | - |
Alcaligenes sp. | 4-Chlorobenzoyl-CoA + AMP + diphosphate | - |
? | |
6.2.1.33 | 4-Chlorobenzoate + CoA + ATP | the rate-limiting step in CBL catalysis follows the formation of 4-chlorobenzoate-CoA | Alcaligenes sp. | 4-Chlorobenzoyl-CoA + AMP + diphosphate | - |
? | |
6.2.1.33 | 4-Methylbenzoate + CoA + ATP | - |
Alcaligenes sp. | 4-Methylbenzoyl-CoA + AMP + diphosphate | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
6.2.1.33 | More | domain and active site structure, overview | Alcaligenes sp. |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
6.2.1.33 | 4-Chlorobenzoate:coenzyme A ligase | - |
Alcaligenes sp. |
6.2.1.33 | CBL | - |
Alcaligenes sp. |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
6.2.1.33 | 25 | - |
assay at | Alcaligenes sp. |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
6.2.1.33 | 7.5 | - |
assay at | Alcaligenes sp. |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
6.2.1.33 | ATP | - |
Alcaligenes sp. |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
6.2.1.33 | additional information | - |
additional information | inhibition kinetics, overview | Alcaligenes sp. |